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Phallacidin

(Synonyms: 羧基二羟鬼笔毒肽) 目录号 : GC44617

A probe for F-actin

Phallacidin Chemical Structure

Cas No.:26645-35-2

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1mg
¥2,998.00
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产品描述

Phallacidin is a natural mycotoxin first isolated from the death cap mushroom, A. phalloides. It binds filamentous actin (F-actin) like phalloidin , but contains a carboxyl group for coupling reactions.

Chemical Properties

Cas No. 26645-35-2 SDF
别名 羧基二羟鬼笔毒肽
Canonical SMILES O=C1[C@@]([H])(NC([C@]([C@H](O)C(O)=O)([H])NC([C@H](C(C)C)NC([C@@H]2CC(C)(O)CO)=O)=O)=O)CSC(NC3=C4C=CC=C3)=C4C[C@@H](C(N2)=O)NC([C@H](C)NC([C@@]5([H])N1C[C@@H](O)C5)=O)=O
分子式 C37H50N8O13S 分子量 846.9
溶解度 DMF: Soluble,DMSO: Soluble,Methanol: Soluble,Water: Soluble 储存条件 Store at -20°C
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1 mM 1.1808 mL 5.9039 mL 11.8078 mL
5 mM 0.2362 mL 1.1808 mL 2.3616 mL
10 mM 0.1181 mL 0.5904 mL 1.1808 mL
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Research Update

Phallacidin stains the mitotic spindle of the diatom Pinnularia spp

Cell Biol Int 2004;28(8-9):565-9.PMID:15350590DOI:10.1016/j.cellbi.2004.04.010.

Mitotic spindles of the diatom Pinnularia viritiformis stained with the fluorescent actin-labelling reagent bodipyphallacidin revealed actin among the chromosomes and extending along the spindle to the poles. This is the first report of actin's presence within spindles of this ecologically important group of organisms. Since diatom mitoses have a number of marked differences compared to that of many other eukaryotes (Int Rev Cytol 128 (1991) 63; Cell 14 (1978) 455), the present observations substantially extend the diversity of mitotic spindle types in which there is evidence of spindle actin.

Phallacidin prevents thrombin-induced increases in endothelial permeability to albumin

Am J Physiol 1989 Sep;257(3 Pt 1):C562-7.PMID:2782396DOI:10.1152/ajpcell.1989.257.3.C562.

Calf pulmonary artery endothelial monolayers cultured on polycarbonate filters were utilized to study 125I-labeled albumin permeability and actin filament distribution in response to thrombin challenge. Thirty-minute exposure to alpha-thrombin (10(-7) M) significantly increased albumin clearance rates. These changes were associated with marked alterations in actin filament distribution, resulting in loss of peripheral actin bands and an increase in the number of cytoplasmic stress fibers. Because the actin peripheral filaments are thought to play an important role in junctional stability, we postulated that stabilization of actin filaments should protect against thrombin-induced barrier disruptions. Pretreatment of cells with 0.3 microM 7-nitrobenz-2-oxa-1,3-diazole (NBD)-phallacidin, a specific actin-stabilizing agent, prevented the changes in actin filament distribution and markedly attenuated the increase in albumin permeability. Because of the potential toxicity of phallatoxins, we evaluated the effects of pretreatment on cell viability and growth parameters. There were no differences in viability, seeding efficiency, or doubling times in cells treated with 0.3 microM NBD-phallacidin in comparison to controls. Our data support the hypothesis that actin filaments, particularly peripheral bands, contribute significantly to the maintenance of barrier function in cultured endothelial cells.

Cytotoxicity on L1210 leukemic cells of beta-amanitin-concanavalin A and phallacidin-concanavalin A conjugates

Toxicon 1990;28(11):1360-3.PMID:2087697DOI:10.1016/0041-0101(90)90102-d.

The conjugates beta-amanitin-concanavalin A and Phallacidin concanavalin A were tested for direct cytotoxicity on L1210 lymphocytic leukemia cells by a combined in vitro-in vivo bioassay. Both conjugates exerted strong direct cytotoxicity on the tumour cells.

Fluorescence staining of the actin cytoskeleton in living cells with 7-nitrobenz-2-oxa-1,3-diazole-phallacidin

Proc Natl Acad Sci U S A 1980 Feb;77(2):980-4.PMID:6928695DOI:10.1073/pnas.77.2.980.

An active fluorescent derivative of the actin-binding mushroom toxin Phallacidin has been synthesized. Convenient methods were developed to stain actin cytoskeletal structures in living and fixed cultured animal cells and actively streaming algal cells. Actin binding specificity was demonstrated by competitive binding experiments and comparative staining of well-known structures. Large populations of living animal cells in culture were readily stained by using a relatively mild lysolecithin permeabilization procedure facilitated by the small molecular size of the label. Actin in animal cells was stained stress fibers, ruffles, the cellular geodome, and in diffuse appearing distributions apparently associated with the plasma membrane. Staining of actin cables in algae with nitrobenzoxadiazole (NBD)-phallacidin did not inhibit cytoplasmic streaming. NBD-phallacidin provides a convenient actin-specific fluorescent label for cellular cytoskeletal structures with promise for use in studies of actin dynamics in living systems.

In vivo staining of cytoskeletal actin by autointernalization of nontoxic concentrations of nitrobenzoxadiazole-phallacidin

J Cell Biol 1981 May;89(2):368-72.PMID:6166616DOI:10.1083/jcb.89.2.368.

The blue light-excited fluorescent phallotoxin derivative nitrobenzoxadiazole Phallacidin (NBD-Ph) was used to stain entire tissue culture monolayers of live L6 mouse cells and other mammalian cell lines without the aid of permeabilization treatment. Although cells tend to exclude the fluorescent toxin, reducing the internal concentration by approximately 1,000 times, some of it enters the cells, probably by pinocytosis, and stains actin structures at low intracellular NBD-Ph concentrations (approximately 5-15 nM), where cell toxicity was negligible or at least not detectable by phase-contrast microscopy. Protracted treatments with NBD-Ph did induce pharmacological responses similar to those of phalloidin. The dissociation constant for NBD-Ph with F-actin in fixed and extracted L6 cells was determined, from staining intensity measurements at various NBD-Ph concentrations, to be 1.5-2.5 x 10(-8) M.